The biosynthesis and secretion of penicillinase and other beta-lactamases by Bacillus licheniformis and Escherichia coli and of the glycoprotein enzymes invertase and carboxypeptidase Y by Saccharomyces yeasts will be studied to determine the various steps in enzyme secretion by microorganisms and its relation to the process in animal cells. We will complete characterization of the hydrophobic substituents on the N-terminus of the membrane penicillinase of B. licheniformis 749/C. The antibiotic globomycin will be used as a probe to detect similar lipophilic beta-lactamases in other species. The synthesis of alpha-amylase by B. licheniformis will be examined for similarities to system producing the 749/C penicillinase. Cloning of the invertase gene (SUC1) and of carboxypeptidase is underway, and favorable preliminary results will be exploited. Chemical studies on the large and small forms of invertase will be continued in parallel with the cloning.